CLM7_MOUSE
ID CLM7_MOUSE Reviewed; 209 AA.
AC Q3U497; Q1ED86; Q3TCP3; Q6SJQ1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=CMRF35-like molecule 7;
DE Short=CLM-7;
DE AltName: Full=CD300 antigen-like family member B;
DE AltName: Full=Immune receptor expressed on myeloid cells 3;
DE Short=IREM-3;
DE AltName: Full=Leukocyte mono-Ig-like receptor 5;
DE AltName: CD_antigen=CD300b;
DE Flags: Precursor;
GN Name=Cd300lb; Synonyms=Irem3, Lmir5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=14662855; DOI=10.4049/jimmunol.171.12.6541;
RA Chung D.-H., Humphrey M.B., Nakamura M.C., Ginzinger D.G., Seaman W.E.,
RA Daws M.R.;
RT "CMRF-35-like molecule-1, a novel mouse myeloid receptor, can inhibit
RT osteoclast formation.";
RL J. Immunol. 171:6541-6548(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=16920917; DOI=10.4049/jimmunol.177.5.2819;
RA Martinez-Barriocanal A., Sayos J.;
RT "Molecular and functional characterization of CD300b, a new activating
RT immunoglobulin receptor able to transduce signals through two different
RT pathways.";
RL J. Immunol. 177:2819-2830(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INTERACTION WITH TYROBP AND HCST, AND FUNCTION.
RC STRAIN=C57BL/6J, and CBA/J; TISSUE=Mast cell;
RX PubMed=17928527; DOI=10.1182/blood-2007-04-085787;
RA Yamanishi Y., Kitaura J., Izawa K., Matsuoka T., Oki T., Lu Y., Shibata F.,
RA Yamazaki S., Kumagai H., Nakajima H., Maeda-Yamamoto M., Tybulewicz V.L.J.,
RA Takai T., Kitamura T.;
RT "Analysis of mouse LMIR5/CLM-7 as an activating receptor: differential
RT regulation of LMIR5/CLM-7 in mouse versus human cells.";
RL Blood 111:688-698(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-203.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Acts as an activating immune receptor in mast cells through
CC its interaction with ITAM-bearing adapter TYROBP.
CC {ECO:0000269|PubMed:17928527}.
CC -!- SUBUNIT: Interacts with TYROBP, which enhances cell surface expression
CC and activation properties. May interact with HCST.
CC {ECO:0000269|PubMed:17928527}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17928527};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:17928527}.
CC -!- TISSUE SPECIFICITY: Expressed in myeloid cells (at protein level).
CC {ECO:0000269|PubMed:17928527}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17928527}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32536.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BC107351; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY457053; AAR27944.1; -; mRNA.
DR EMBL; AY996128; AAY56360.1; -; mRNA.
DR EMBL; AB300703; BAF56590.1; -; mRNA.
DR EMBL; AK154359; BAE32536.1; ALT_INIT; mRNA.
DR EMBL; AK170613; BAE41912.1; -; mRNA.
DR EMBL; AL669969; CAM18752.1; -; Genomic_DNA.
DR EMBL; AL607025; CAM18752.1; JOINED; Genomic_DNA.
DR EMBL; BC107351; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS25614.2; -.
DR RefSeq; NP_954691.2; NM_199221.2.
DR AlphaFoldDB; Q3U497; -.
DR SMR; Q3U497; -.
DR STRING; 10090.ENSMUSP00000073913; -.
DR GlyGen; Q3U497; 1 site.
DR iPTMnet; Q3U497; -.
DR PhosphoSitePlus; Q3U497; -.
DR PaxDb; Q3U497; -.
DR PRIDE; Q3U497; -.
DR ProteomicsDB; 283307; -.
DR Antibodypedia; 53132; 112 antibodies from 21 providers.
DR DNASU; 217304; -.
DR Ensembl; ENSMUST00000239005; ENSMUSP00000159146; ENSMUSG00000063193.
DR GeneID; 217304; -.
DR KEGG; mmu:217304; -.
DR UCSC; uc007mgb.1; mouse.
DR CTD; 124599; -.
DR MGI; MGI:2685099; Cd300lb.
DR VEuPathDB; HostDB:ENSMUSG00000063193; -.
DR eggNOG; ENOG502S7MA; Eukaryota.
DR GeneTree; ENSGT00940000162729; -.
DR HOGENOM; CLU_051023_3_1_1; -.
DR InParanoid; Q3U497; -.
DR OMA; IYWCGIQ; -.
DR OrthoDB; 1494510at2759; -.
DR PhylomeDB; Q3U497; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2172127; DAP12 interactions.
DR BioGRID-ORCS; 217304; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q3U497; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3U497; protein.
DR Bgee; ENSMUSG00000063193; Expressed in granulocyte and 55 other tissues.
DR ExpressionAtlas; Q3U497; baseline and differential.
DR Genevisible; Q3U497; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0002446; P:neutrophil mediated immunity; IMP:MGI.
DR GO; GO:0033005; P:positive regulation of mast cell activation; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..209
FT /note="CMRF35-like molecule 7"
FT /id="PRO_0000320131"
FT TOPO_DOM 18..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..120
FT /note="Ig-like V-type"
FT SITE 164
FT /note="Interaction with TYROBP"
FT /evidence="ECO:0000250"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..104
FT /evidence="ECO:0000250"
FT VARIANT 203..209
FT /note="LAKDISP -> SS (in strain: C57BL/6)"
FT CONFLICT 19
FT /note="Q -> P (in Ref. 3; AAY56360)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="M -> R (in Ref. 3; AAY56360)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="R -> S (in Ref. 3; AAY56360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 23755 MW; 7D39A85C0B731CFD CRC64;
MWLSPALLLL SFPGCLSIQG PALVRGPEQG SVTVQCRYSS RWQTNKKWWC RGASWSTCRV
LIRSTGSEKE TKSGRLSIRD NQKNHSFQVT MEMLRQNDTD TYWCGIEKFG TDRGTRVKVN
VYSVGKDTMS TSNQLPWPTV DGSTDMVSSD LQKRTYYMLL VFVKVPALLI LVGAVLWLKR
STQKVPEEQW RHTLCSDLDS ELLAKDISP
